Abstract
Various types of channels vary their function by membrane tension changes upon cellular activities, and lipid bilayer methods allow elucidation of direct interaction between channels and the lipid bilayer. However, the dynamic responsiveness of the channel to the membrane tension remains elusive. Here, we established a time-lapse tension measurement system. A bilayer is formed by docking two monolayer-lined water bubbles, and tension is evaluated via measuring intrabubble pressure as low as <100 Pa (Young-Laplace principle). The prototypical KcsA potassium channel is tension-sensitive, and single-channel current recordings showed that the activation gate exhibited distinct tension sensitivity upon stretching and relaxing. The mechanism underlying the hysteresis is discussed in the mode shift regime, in which the channel protein bears short "memory" in their conformational changes.